Quantification of Peptide Bond Types in Human Proteome Indicates How DNA Codons were Assembled at Prebiotic Conditions
- *Corresponding Author:
- Dr. Joaef Nahalka
Institute of Chemistry, Center for Glycomics
Slovak Academy of Sciences, Dúbravská cesta 9
SK-84538 Bratislava, Slovak Republic
E-mail: [email protected]
Received Date: July 23, 2011; Accepted Date: August 23, 2011; Published Date: August 25, 2011
Citation: Nahalka J (2011) Quantification of Peptide Bond Types in Human Proteome Indicates How DNA Codons were Assembled at Prebiotic Conditions. J Proteomics Bioinform 4: 153-159. doi:10.4172/jpb.1000184
Copyright: © 2011 Nahalka J. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
[GADV]-protein world hypothesis  leaded me to quantification of decapeptides assembled from G, A, V, D in human proteome. The G, A, V, and D amino acids were related to the nucleotides Guanine (g), Cystosine (c), Uracil (u), and Adenine (a). The search revealed agreement with the genetic code. The types of prebiotic peptide bonds represent probably the first selection power that established the base order in the codons. The genetic code underwent three phases of formation, which explain why modern codons have their particular order of nucleotides: the monobase, dibase and the modern phase (tribase). Sequence alignments and 3D structures of aminoacyl-tRNA synthetases confirm the depicted picture of “relatedness” and the picture indicates how “relatedness” is used by aminoacyl-tRNA synthetases for navigation into and within of the C-terminal anticodon-binding domain. The findings presented here illustrate the novel concept of possible translation of the amino acid sequence into a nucleotide sequence that can be in interactive or contrary mode regarding to desired protein-RNA interactions. Hopefully, it could be used in synthetic biology.